1dfa
From Proteopedia
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| - | [[Image:1dfa.gif|left|200px]] | + | [[Image:1dfa.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF PI-SCEI IN C2 SPACE GROUP''' | + | {{Structure |
| + | |PDB= 1dfa |SIZE=350|CAPTION= <scene name='initialview01'>1dfa</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF PI-SCEI IN C2 SPACE GROUP''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DFA is a [ | + | 1DFA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFA OCA]. |
==Reference== | ==Reference== | ||
| - | Probing the structure of the PI-SceI-DNA complex by affinity cleavage and affinity photocross-linking., Hu D, Crist M, Duan X, Quiocho FA, Gimble FS, J Biol Chem. 2000 Jan 28;275(4):2705-12. PMID:[http:// | + | Probing the structure of the PI-SceI-DNA complex by affinity cleavage and affinity photocross-linking., Hu D, Crist M, Duan X, Quiocho FA, Gimble FS, J Biol Chem. 2000 Jan 28;275(4):2705-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10644733 10644733] |
[[Category: H(+)-transporting two-sector ATPase]] | [[Category: H(+)-transporting two-sector ATPase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: intein]] | [[Category: intein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:37:36 2008'' |
Revision as of 08:37, 20 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF PI-SCEI IN C2 SPACE GROUP
Overview
The PI-SceI protein is an intein-encoded homing endonuclease that initiates the mobility of its gene by making a double strand break at a single site in the yeast genome. The PI-SceI protein splicing and endonucleolytic active sites are separately located in each of two domains in the PI-SceI structure. To determine the spatial relationship between bases in the PI-SceI recognition sequence and selected PI-SceI amino acids, the PI-SceI-DNA complex was probed by photocross-linking and affinity cleavage methods. Unique solvent-accessible cysteine residues were introduced into the two PI-SceI domains at positions 91, 97, 170, 230, 376, and 378, and the mutant proteins were modified with either 4-azidophenacyl bromide or iron (S)-1-(p-bromoacetamidobenzyl)-ethylenediaminetetraacetate (FeBABE). The phenyl azide-coupled proteins cross-linked to the PI-SceI target sequence, and the FeBABE-modified proteins cleaved the DNA proximal to the derivatized amino acid. The results suggest that an extended beta-hairpin loop in the endonuclease domain that contains residues 376 and 378 contacts the major groove near the PI-SceI cleavage site. Conversely, residues 91, 97, and 170 in the protein splicing domain are in close proximity to a distant region of the substrate. To interpret our results, we used a new PI-SceI structure that is ordered in regions of the protein that bind DNA. The data strongly support a model of the PI-SceI-DNA complex derived from this structure.
About this Structure
1DFA is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Probing the structure of the PI-SceI-DNA complex by affinity cleavage and affinity photocross-linking., Hu D, Crist M, Duan X, Quiocho FA, Gimble FS, J Biol Chem. 2000 Jan 28;275(4):2705-12. PMID:10644733
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